Isolation and partial characterization of grape aminopeptidase

Aminopeptidase from grape berries was purified to homogeneity and partially characterized. The enzyme preparation was stable for several months in 10% glycerol. Aminoacyl- beta -naphthylamides as well as aminoacyl-p-nitroanilides and dipeptides could be hydrolyzed by the enzyme but Leu-Gly-Gly, Gly-...

Full description

Saved in:
Bibliographic Details
Published in:Journal of agricultural and food chemistry 1981-11, Vol.29 (6), p.1216-1220
Main Authors: Pallavicini, Cosimo, Peruffo, Angelo Dal Belin, Santoro, Michele
Format: Article
Language:English
Subjects:
aminopeptidase
purification
Vitis vinifera
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Aminopeptidase from grape berries was purified to homogeneity and partially characterized. The enzyme preparation was stable for several months in 10% glycerol. Aminoacyl- beta -naphthylamides as well as aminoacyl-p-nitroanilides and dipeptides could be hydrolyzed by the enzyme but Leu-Gly-Gly, Gly-Gly-Leu, Leu-Gly-Gly-Gly, and carboxypeptidase substrates were not cleaved. The enzyme gave very limited hydrolytic products from casein and grape protein. Its temperature and pH optima were 40 degree C and 7.4, respectively, and the activation energy was 9.5 kcal/mol. SH agents, S-S reducing agents, and diphenylcarbamyl chloride inhibited to varying extents its activity, whereas phenylmethanesulfonyl fluoride exhibited a poor effect. The molecular weight of the enzyme was estimated to be 95,000. By disc electrophoresis, NaDodSO sub(4) electrophoresis, and isoelectric focusing on polyacrylamide gels, two variants (M sub(r) 62,000 and 33,000) were detected.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf00108a029